The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"formyl-coa transferase, domain 3
".
FunFam 10: Acyl-CoA transferase/carnitine dehydratase-like pr...
Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
There are 1 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Intramolecular transferase activity, transferring acyl groups GO:0016867
Catalysis of the transfer of an acyl group from one position to another within a single molecule.
|
1 | A9WC36 (/IDA) |
There are 1 GO terms relating to "biological process"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Carbon fixation by 3-hydroxypropionate cycle GO:0043427
An autotrophic carbon dioxide fixation pathway by which two molecules of carbon dioxide are fixed to form glyoxylate. Acetyl coenzyme A (acetyl-CoA) is assumed to be converted to malate, and two CO2 molecules are thereby fixed. Malyl-CoA is thought to be cleaved to acetyl-CoA, the starting molecule, and glyoxylate, the carbon fixation product.
|
1 | A9WC36 (/IDA) |
There are 0 GO terms relating to "cellular component"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.